Polishing Methods for Monoclonal IgG Purification

Keyword(s):  
2017 ◽  
Vol 38 (22-23) ◽  
pp. 2914-2921 ◽  
Author(s):  
Foad Tehrani Najafian ◽  
Noor Shad Bibi ◽  
Tuhidul Islam ◽  
Marcelo Fernández-Lahore

2012 ◽  
Vol 42 (6) ◽  
pp. 598-610 ◽  
Author(s):  
Yu Yi ◽  
Li Zhu ◽  
Jianfeng Mei ◽  
Jianshu Chen ◽  
Guoqing Ying
Keyword(s):  

2020 ◽  
Author(s):  
Ramesh K. Jha ◽  
Allison Yankey ◽  
Kalifa Shabazz ◽  
Leslie Naranjo ◽  
Nileena Velappan ◽  
...  

ABSTRACTWhile natural protein-protein interactions have evolved to be induced by complex stimuli, rational design of interactions that can be switched-on-demand still remain challenging in the protein design world. Here, we demonstrate a computationally redesigned natural interface for improved binding affinity could further be mutated to adopt a pH switchable interaction. The redesigned interface of Protein G-IgG Fc domain, when incorporated with histidine and glutamic acid on Protein G (PrG-EHHE), showed a switch in binding affinity by 50-fold when pH was altered from mild acidic to mild basic. The wild type (WT) interface only showed negligible switch. The overall binding affinity at mild acidic pH for PrG-EHHE outperformed the WT PrG interaction. The new reagent PrG-EHHE will be revolutionary in IgG purification since the traditional method of using an extreme acidic pH for elution can be circumvented.Abstract Figure


2012 ◽  
Vol 30 (8-9) ◽  
pp. 701-711 ◽  
Author(s):  
Diego R. Gondim ◽  
Luana P. Lima ◽  
Maria C. M. de Souza ◽  
Igor T. L. Bresolin ◽  
Wellington S. Adriano ◽  
...  

2010 ◽  
Vol 878 (23) ◽  
pp. 2087-2093 ◽  
Author(s):  
Igor Tadeu Lazzarotto Bresolin ◽  
Maria Cristiane Martins de Souza ◽  
Sonia Maria Alves Bueno

2010 ◽  
Vol 348 (1-2) ◽  
pp. 224-230 ◽  
Author(s):  
Telma Barroso ◽  
Márcio Temtem ◽  
Abid Hussain ◽  
Ana Aguiar-Ricardo ◽  
Ana C.A. Roque

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